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Modulation of α-Synuclein Aggregation In Vitro by a DNA Aptamer.

Claire H Tran1, Ranajay Saha2, Celia Blanco2

  • 1Program in Biomolecular Sciences and Engineering, Department of Chemistry and Biochemistry, University of California, Santa Barbara, California 93106, United States.

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|August 22, 2022
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Summary
This summary is machine-generated.

Nucleic acid aptamers can inhibit protein aggregation. This study shows an aptamer stabilizing off-pathway aggregates, offering a novel mechanism for modulating protein aggregation in diseases like synucleinopathies.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biotechnology

Background:

  • Protein aggregation is implicated in human diseases and impacts biotechnology.
  • Modulating protein aggregation is crucial for therapeutic and production applications.
  • Nucleic acid aptamers are potential agents for controlling protein aggregation.

Purpose of the Study:

  • To investigate the mechanism by which aptamers modulate alpha-synuclein aggregation.
  • To characterize the effect of the T-SO508 aptamer on alpha-synuclein aggregation in vitro.

Main Methods:

  • In vitro aggregation kinetics monitored by thioflavin T.
  • Characterization of intermediate structures using atomic force microscopy, transmission electron microscopy, and analytical ultracentrifugation.

Main Results:

  • The T-SO508 aptamer extended the lag phase of alpha-synuclein aggregation.
  • T-SO508 stabilized small, non-fibrillar alpha-synuclein aggregate complexes.
  • These aptamer-induced complexes were found to be off-pathway for fibril formation.

Conclusions:

  • Aptamers can modulate protein aggregation by stabilizing off-pathway intermediates.
  • This mechanism provides insight into aptamer-based therapeutic strategies for protein aggregation disorders.
  • The findings highlight a potential role for aptamers in managing synucleinopathies.